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      Penapisan Lektin dari Alga Hijau Asal Pantai Sepanjang, Y ogyakarta dan Binuangeun, Banten

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      Date
      2015
      Author
      Fahriza, Anisa
      Ariyanti., Nunik Sri
      Nurahmi Dewi F.
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      Abstract
      Lectins are carbohydrate binding proteins that are reversible and have ability to agglutinate. Lectins derived from algae have several advantages, such as having low molecular mass, able to bind specific complex oligosaccharides and glycoproteins and they do not require divalent cations for their biological activity. This research aims to screen lectins of green algae from the coastal of Sepanjang, Yogyakarta and Binuangeun, Banten. This research consists of four stages: 1) sampling and identification of green algae; 2) extraction of the algal sample using Tris Buffer Saline (TBS) and Phosphate Buffer Saline (PBS); 3) hemagglutination test of the crude extract using rabbit eritrocytes and group A, B, and O of human eritrocytes, both native and enzyme treated erithrocytes; 4) analysis of total protein content using the BCA protein assay kits. Eleven species of green algae were collected and extracted. Five species of the algae (Cladhopora patentiramea, Ulva fasciata, Halimeda macroalba, Caulerpa racemosa var. macrophysa, dan Halimeda micronesica) showed hemagglutination activity on human erithrocytes. However, hemagglutination test of the other species (Ulva reticulata, Caulerpa sertulaioides, Caulerpa racemosa var. peltata, Chaetopmorha crassa, Enteromorpha intestinalis, dan morfospecies 1.) showed negative result on human erithrocytes. The hemagglutination activity of all the algae was positive on rabbit erithrocytes. Hemagglutination activity of all the algae except Ulva fasciata and Halimeda macroalba on the trypsin treated erithrocytes was lower than the native erithrocytes. A total of 5 species of green algae which showed activity against human erythrocytes, specifically on either O, A, and B blood group. The high total protein content of the algal extract did not positively correlated with the hemagglutination activity.
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      http://repository.ipb.ac.id/handle/123456789/76028
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